99 results about "Recombinant peptide" patented technology

The present invention provides a composition including an isolated or recombinant peptide component that has osteogenic cell proliferative activity. The peptide, which promotes proliferation of osteoblasts, is useful for treatment of fractures, as a filler in deficient sites of bone, for inhibition of decrease in bone substance related to osteoporosis and periodontic diseases, and for prevention of fractures associated with osteoporosis and rheumatoid arthritis. The peptide, or cells that have been genetically engineered to produce the peptide, can be combined with a bone-compatible matrix to facilitate slow release of the peptide to a treatment site and/or provide a structure for developing bone.

Use of a polypeptide or protein with amino acid sequence corresponding substantially to AFP-type III HPLC 12 as additive in a product for improvement of said product, said improvement residing in improved properties of modification of ice crystal growth processes influencing size and shape characteristics of ice in particular in regrowth thereby e.g. minimising potential freezing damage e.g. by preventing or inhibiting ice recrystallisation of the product upon freezing, said use occurring in a manner known per se for anti freeze peptides to obtain higher specific modification activity in particular antifreeze activity than obtainable with the same amount of Winter Flounder AFP.

The present invention provides a method for purifying recombinant peptides, polypeptides or proteins away from truncated or other full-length forms of these molecules. In particular the invention contemplates a method of purifying a vascular endothelial growth factor (VEGF) molecule by subjecting a biological sample containing the molecule to be purified to affinity chromatography under conditions sufficient for the full length molecules to bind and not the truncated or clipped forms. In the preferred embodiment there are two columns, the first is based on affinity for a poly his tag, the second column based on heparin binding affinity. Particularly preferred VEGF molecules are untagged VEGF-B₁₆₇, hexa-His-tagged VEGF-B₁₆₇, hexa-His-tagged VEGF-B₁₈₆ and hexa-His-tagged VEGF-B_10-108.

An intracellular selection system allows concurrent screening for peptide bioactivity and stability. Randomized recombinant peptides are screened for bioactivity in a tightly regulated expression system, preferably derived from the wild-type lac operon. Bioactive peptides thus identified are inherently protease- and peptidase-resistant. Also provided are bioactive peptides stabilized by a stabilizing group at either the N-terminus, the C-terminus, or both. The stabilizing group can take the form of a small stable protein, such as the Rop protein, glutathione sulfotransferase, thioredoxin, maltose binding protein, or glutathione reductase, or one or more proline residues.

The present invention provides recombinant peptides that specifically and selectively bind to the human milk fat globule (HMFG) antigen, BA46. In particular, the present invention provides recombinant variants of the Mc3 antibody, including humanized versions of Mc3. The variant Mc3 peptides are particularly useful for diagnostic, prognostic, and therapeutic applications in the field of breast cancer. The present invention also provides methods for the humanization of antibodies such as murine monoclonal antibodies. The novel humanization methods are applied to the production of humanized Mc3 antibodies and it is shown that these humanized antibodies retain the ability to engage in high affinity binding to their cognate antigen. Such humanization enables the use of these antibodies for immunodiagnostic and immunotherapeutic applications in humans.

The invention relates to a compound immunological adjuvant comprising a water phase solution and an oil phase solution which are respectively prepared, wherein the water phase solution is a CpG water solution the concentration of which is 0.5 to 2.0mg/mL; the oil phase solution is an imiquimod white oil solution the concentration of which is 0.25 to 1.0mg/mL; and the volume ratio of the water phase solution to the oil phase solution is 1:6. The invention also relates to a vaccine prepared from one or more antigens selected from attenuated live full microorganisms, inactivated microorganisms, recombinant peptide and proteins, synthetic peptide and cracked microorganisms and the water phase solution and the oil phase solution in the compound immunological adjuvant according to the volume ratio of 1:1:6. By the compounding of imiquimod, CpG and a white oil component, the compound immunological adjuvant has an obvious synergistic effect and enhances the immunological activity reactions of Th1 and Th2, so that the activity of stimulated immunological cells is obviously enhanced.

The present invention relates to genetic engineering and; in specific, to design, generation, and modification of recombinant peptides using a combination of phage display and intein-mediated protein cleavage reaction.

The invention constructs recombinant plasmid vector containing tumstatin T7 peptide and gene sequence of derivative T7-NGR thereof and obtains recombinant T7 peptide and T7-NGR fusion protein. The amino acid sequence of the derivative T7-NGR is TMPFLFCNVNDVCNFASRNDYSYWLGSCNGRCVSGCAGRC. The invention combines the generation activity of tumstatin T7 peptide for restricting the tumor neovascularization effectively and high specificity of NGR guide peptide, so as to lead the generation activity of T7 peptide for restricting the tumor neovascularization to be greatly strengthened. The recombinant cloned vectors are respectively identified by sequencing: the direction, position and sequence of integration are correct. The expression vector is transformed into competent E.coli BL21 (DE3) and then is expressed by the induction of IPTG; electrophoresis is carried out on the thalli after cracking; and by Western-Blot identification, the expression product is in accordance with the expected. The pET7N expression vector fusion protein T7-NGR has potential application prospect in the diagnosis and treatment of tumor.

The present invention provides improved methods for the production of recombinant peptides from bacterial cells.

The invention relates to the recombinant expression of a peptide of interest in the form of a fusion protein comprising a solubility tag. The fusion protein comprises at least two portions separated by a cleavable peptide sequence wherein one portion is devoid of cysteine residues and the second portion comprises an effective number of cross-linkable cysteine residues. After cell lysis and isolation of the fusion protein, the fusion protein is subsequently cleaved into a mixture of first and second portions. Oxidative cross-linking is used to selectively precipitate one of the two portions to facilitate simple and effective separation of the peptide of interest.

The present invention relates to a method for producing a recombinant, spider toxin peptide and analgesic compositions containing said peptide. More specifically, the present invention relates to a method in which the gene for GsMTx4 is subcloned into a vector, so that it is linked to a secretion signal sequence of the alpha factor and under the control of methanol-inducible alcohol oxidase (AOX) promoter to construct a recombinant yeast expression plasmid. Yeast cells are transformed with this plasmid to produce the GsMTx4 peptide and analgesic compositions containing said peptide. The recombinant yeast expression system of the present invention affords a more stable method for producing GsMTx4 than its natural route. Thus the GsMTx4 peptide and its derivatives produced by the method of this invention can be used in the cure of related diseases such as heart failure as the peptide specifically inhibits mechanosensitive ion channels.

The present invention addresses the problem of providing: a posterior silk gland gene expression unit, whereby a recombinant peptide, in particular a water-soluble peptide, can be expressed in a large amount in the posterior silk gland of a silkworm such as Bombyx mori; and a transgenic silkworm into which the aforesaid gene expression unit has been transferred. Provided is a posterior silk gland gene expression unit which comprises: a promoter of a gene encoding a protein, said protein being expressed specifically in the posterior silk gland; a DNA encoding a signal peptide originating in a protein, said protein being expressed specifically in the middle silk gland, functionally bound to the downstream of the promoter; and a DNA encoding a target peptide, said peptide being free from proteins secreted as constituents of fibroin, ligated to the downstream thereof.

The present invention provides methods for producing recombinant peptides in a bacterial host utilizing a mannitol, arabitol, glucitol, or glycerol-inducible promoter, wherein the host bacterial cell that produces the peptide has been rendered incapable of degrading or metabolizing mannitol, arabitol, or glucitol, or derivatives or analogues thereof. The present invention provides bacterial cells that have been genetically altered to inhibit the metabolism or degradation of mannitol, glucitol, or arabitol, or derivatives or analogues thereof. The present invention utilizes mannitol, arabitol, glucitol, or glycerol to induce expression of a target polypeptide from an inducible promoter, allowing for the use of an inexpensive and stable carbon source inducer in the fermentation processes for the production of recombinant peptides.

Peptides are produced as fusions with a suitable carrier protein. The carrier protein disclosed herein are adapted from the N-terminal domain of staphylococcus nuclease. This novel carrier protein acts to promote the over-expression of the peptide-protein fusion in the form of inclusion bodies, which minimizes in-cell proteolysis of desired peptides. The fusion protein is readily purified by conventional procedures or His-tag affinity chromatography when His-tag is inserted into the fusion protein. The target peptide is released from the purified fusion protein by a simple cleavage step and separated from the librated carrier protein by use of a reverse-phase HPLC process or by repeating the same affinity purification method. A particular advantage of the disclosed method, in addition to the obvious advantage of high yields, is its use for producing isotopically labeled peptides for NMR characterization of bioactive peptides and their interactions with target proteins.

The present invention discloses an improved process for the production of desired recombinant peptides from bacterial cells by using G-CSF as a novel fusion partner for their high level expression in these cells. The invention further provides an expression system comprising the fusion protein wherein the G-CSF is operatively linked to the peptide of interest via an enzymatic or chemical cleavage site which can be used to separate the fusion partner from the said peptide.